Folding pathway mediated by an intramolecular chaperone.

@article{Shinde1993FoldingPM,
  title={Folding pathway mediated by an intramolecular chaperone.},
  author={Ujwal Shinde and Yunge Li and Sugata Chatterjee and M. Inouye},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 15},
  pages={6924-8}
}
The N-terminal propeptide of subtilisin, a serine protease, functions as an intramolecular chaperone which is crucial for proper folding of the active enzyme. This nascent N-terminal propeptide is removed after completion of the folding process. Here we present a possible pathway by which intramolecular chaperones mediate protein folding. Using circular dichroism to analyze acid-denatured subtilisin we have identified a folding-competent state which can refold to an active conformation in the… CONTINUE READING

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